A chemical system which uses the enzyme peroxidase, donor molecules and peroxide in an aqueous environment is taught in U.S. Pat. Nos. 4,476,108; 4,473,550; and 4,588,586. When the donor molecule is iodide peroxidase will catalyze the reduction of hydrogen peroxide to water with the concomitant oxidation of iodide anions. This system enzymatically generates an aqueous environment with reaction products and reaction by-products that inactivate pathogenic organisms. The solution generated with this chemistry contains; (1) the enzyme generated actives, (2) iodide at levels that are reduced from the initial concentration, (3) peroxide at levels that are reduced from the initial concentration, and (4) the protein peroxidase at the initial use concentration.
Peroxidases can be isolated from a variety of sources and their properties vary as a function of the source. The molecular weight of peroxidases ranges from 12,000 daltons for NADH peroxidase to 149,000 daltons for mycloperoxidase. The peroxidase as taught in U.S. Pat. Nos. 4,476,108; 4,473,550; and 4,588,586 is a peroxidase which falls under the Enzyme Commission's (E.C.) classification of 1.11.1.7. Practical considerations of cost and stability favor horseradish peroxidase as the preferred peroxidase within the E.C.I. 1.11.1.7 classification. Horseradish peroxidase has a molecular weight of about 40,000 daltons.
Peroxidases, with a few exceptions such as mycloperoxidase and cytochrome c peroxidase, are glycoproteins. Glycoproteins with a molecular weight greater than 10,000 daltons are known to act as immunogens in animals. Horseradish peroxidase is known to be an effective immunogen and it is possible to purchase antibodies to this protein commercially. In fact peroxidase-anti-peroxidase soluble complexes are sold as a reagent and used in (1) immunohistological applications on frozen or paraffin embedded tissue sections, (2) electron microscopy and (3) immunoblots. Both polyclonal and monoclonal antibodies are available to horseradish peroxidase.
Repeated contact of peroxidase with a wound or tissue could cause the formation of antiperoxidase antibodies. Once anti-peroxidase antibodies are formed within an animal, subsequent exposure to peroxidase could cause an allergic reaction. Such an allergic reaction can take the full spectrum of immediate and delayed types of allergic reactions produced by foreign macmomolecules. These reactions include exfoliative dermatitis, urticaria and angiodema, fever, asthma and even anaphylaxis.
It is obvious that a disinfectant that comes into contact, whether directly or indirectly, with animal or human wounds, tissues or organs should not contain immunogenic proteins. Therefore, peroxidase immunogenicity argues against such a use for the formulations described in the above mentioned patents. This application describes a method to form the active chemistry described in U.S. Pat. Nos. 4,476,108; 4,473,550; and 4,588,586 while minimizing or eliminating the potential for allergic reactions in animals and humans. The methods described in this application are effective against bacteria, fungi, spores and viruses.